| Literature DB >> 16511198 |
Taku Ohki1, Nobuhiro Mizuno, Naoki Shibata, Masahiro Takeo, Seiji Negoro, Yoshiki Higuchi.
Abstract
To investigate the structure-function relationship between 6-aminohexanoate-dimer hydrolase (EII) from Arthrobacter sp. and a cryptic protein (EII') which shows 88% sequence identity to EII, a hybrid protein (named Hyb-24) of EII and EII' was overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant in MES buffer pH 6.5. The crystal belongs to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.37, c = 113.09 A. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 A, respectively.Entities:
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Year: 2005 PMID： 16511198 PMCID： PMC1991307 DOI： 10.1107/S1744309105028812
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091